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  • 2-dimensional correlation analysis  (1)
  • 62F15  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Theory and decision 40 (1996), S. 191-214 
    ISSN: 1573-7187
    Keywords: 62J99 ; 62F15 ; 62C10 ; 62C15 ; Utility theory ; non-informative prior ; distributional distance ; entropy ; Hellinger distance ; conjugate prior ; Fisher information ; exponential families ; bayes estimator
    Source: Springer Online Journal Archives 1860-2000
    Topics: Sociology , Economics
    Notes: Abstract Since the choice of a particular loss function strongly influences the resulting inference, it seems necessary to rely on “intrinsic” losses when no information is available about the utility function of the decision-maker, rather than to call for classical losses like the squared error loss. Since this setting is quite similar to the derivation of noninformative priors in Bayesian analysis, we first recall the conditions of this derivation and deduce from these conditions some requirements on the intrinsic losses. It then appears that these loss functions should only depend on the sampling distribution and that they should be independent of the parameterization of the distribution. The resulting estimators are therefore transformation equivariant. We study the properties of two natural intrinsic losses, namely entropy and Hellinger losses, and show that they can be expressed in closed form for exponential families. Moreover, the entropy loss also provides analytic expressions of Bayes estimators under conjugate priors; the derivation of Bayes estimators associated with the Hellinger loss is more cumbersome, as shown in Poisson and Gamma cases, while leading to similar estimators.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1075-4261
    Keywords: near-IR ; protein folding ; denaturation ; ribonuclease A ; overtone and combination bands ; 2-dimensional correlation analysis ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: We introduce near-IR spectroscopy as an ancillary tool for monitoring structural changes of proteins in aqueous solution using ribonuclease A (RNase A) as a model protein. The thermal unfolding of RNase A results in clear spectral changes in the near-IR and the mid-IR regions. In the near-IR the most pronounced changes are observed in the spectral region between 4820 and 4940 cm-1. The strong N—H combination band found at 4867 cm-1 in the spectrum of native RNase A shifts to 4878 cm-1 upon thermal unfolding. Hydrogen-deuterium exchange experiments that validate the N—H character of this mode can also be used to estimate the number of unexchanged amide protons after exposure to D2O. The transition profiles and temperatures derived from the temperature dependence of the N—H combination mode were found to be practically identical with those derived from the temperature dependence of the C=O amide I band in the mid-IR region, demonstrating that the near-IR region can be used as a conformation-sensitive monitor for the thermally induced unfolding of proteins in H2O solution. A 2-dimensional correlation analysis was applied to the mid-IR and near-IR spectra of RNase A to establish correlations between IR bands in both regions. The correlation analysis demonstrates that the thermal unfolding of RNase A is not a completely cooperative process; rather it begins with some changes in β-sheet structure, followed by the loss of α-helical structures, and then ending with the unfolding of the remaining β-sheets. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S19-S29, 1998
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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